Hemorphin and hemorphin-like peptides isolated from dog pancreas and sheep brain are able to potentiate bradykinin activity in vivo

Peptides

Volumn 27, Issue 11, 2006, Pages 2957-2966

  Ianzer, Danielle ^a   Konno, Katsuhiro ^a   Xavier, Carlos Henrique ^b   Stöcklin, Reto ^c   Santos, Robson Augusto S ^b   de Camargo, Antônio Carlos Martins ^a   Pimenta, Daniel Carvalho ^a  

^a CAT CEPID   (Brazil)

^b ICB   (Brazil)

^c ATHERIS LABORATORIES   (Switzerland)

Author keywords

Bradykinin; Bradykinin potentiating peptide; De novo sequencing; Hemoglobin; Hemorphin; Mass spectrometry

Indexed keywords

HEMORPHIN 7; PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG; VASOACTIVE AGENT;

AMINO ACID SEQUENCE; ANIMAL TISSUE; ANTIHYPERTENSIVE ACTIVITY; ARTICLE; BIOLOGICAL ACTIVITY; BIOLOGICAL MONITORING; BLOOD PRESSURE REGULATION; BRAIN HOMOGENATE; DOG; EXPERIMENTAL RAT; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; IN VIVO STUDY; MAMMAL; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN ISOLATION; SHEEP;

AMINO ACID SEQUENCE; ANIMALS; BIOLOGICAL ASSAY; BLOOD PRESSURE; BRADYKININ; BRAIN CHEMISTRY; DOGS; DRUG SYNERGISM; FEMALE; GUINEA PIGS; HEMOGLOBINS; ILEUM; MALE; MOLECULAR SEQUENCE DATA; ORGAN CULTURE TECHNIQUES; PANCREAS; PEPTIDE FRAGMENTS; PEPTIDES; RATS; RATS, WISTAR; SHEEP; UP-REGULATION;

CANIS FAMILIARIS; MAMMALIA; OVIS ARIES;

EID: 33750183474     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2006.06.009     Document Type: Article

References (39)

1. Aliste M.P., MacCallum J.L., and Tieleman D.P. Molecular dynamics simulations of pentapeptides at interfaces: salt bridge and cation-pi interactions. Biochemistry 42 30 (2003) 8976-8987
2. Barkhudaryan N., Oberthuer W., Lottspeich F., and Galoyan A. Structure of hypothalamic coronaro-constrictory peptide factors. Neurochem Res 17 (1992) 1217-1221
3. Brantl V., Gramsch C., Lottspeich F., Mertz R., Jaeger K.H., and Hertz A. Novel opioid peptides derived from hemoglobin: hemorphins. Eur J Pharmacol 125 2 (1986) 309-310
4. Brown AG, Leite RS, Engler AJ, Discher DE, Strauss III JF. A hemoglobin fragment found in cervicovaginal fluid from women in labor potentiates the action of agents that promote contraction of smooth muscle cells. Peptides 2006 [Epub ahead of print].
5. Čejka J., Železná1 B., Velek J., Zicha J., and Kuneš J. LVV-hemorphin-7 lowers blood pressure in spontaneously hypertensive rats: radiotelemetry study. Physiol Res 53 (2004) 603-607
6. Chagas J.R., Juliano L., and Prado E.S. Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins. Anal Biochem 192 (1991) 419-425
7. Chiba T., Li Y.H., Yamane T., Ogibuko O., Fukukoa M., Arai R., et al. Inhibition of recombinant dipeptidyl peptidase III by synthetic hemorphin-like peptides. Peptides 24 (2003) 773-778
8. Cho J.H., Park I.Y., Kim H.S., Lee W.T., Kim M.S., and Kim S.C. Cathepsin D produces antimicrobial peptide parasin I from histone H2A in the skin mucosa of fish. FASEB J 6 3 (2002) 429-431
9. Choisnard L., Durand D., Vercaigne-Marko D., Nedjar-Arroune N., Dhusler P., and Guillochon D. A simple method for the two-step preparation of two pure haemorphins from a total haemoglobin peptic hydrolysate by conventional low-pressure chromatographies. Biotechnol Appl Biochem 34 (2001) 173-181
10. Cohen M., Fuitier-Arnaudin I., and Piot J.M. Hemorphins: substrates and/or inhibitors of dipeptidyl peptidase IV. Hemorphins N-terminus sequence influence on the interaction between hemorphins and DPPIV. Biochimie 86 (2004) 31-37
11. Dagouassat N., Garreau I., Sannier F., Zhao Q., and Piot J.M. Generation of VV-hemorphin-7 from globin by peritoneal macrophages. FEBS Lett 382 (1996) 37-42
12. Fruitier I., Garreau I., Lacroix A., Cupo A., and Piot J.M. Proteolytic degradation of hemoglobin by endogenous lysosomal proteases gives rise to bioactive peptides: hemorphins. FEBS Lett 447 (1999) 81-86
13. Fruitier I., Garreau I., and Piot J.M. Cathepsin D is a good candidate for the specific release of a stable hemorphin from hemoglobin in vivo: VV-hemorphin-7. BBRC 246 (1998) 719-724
14. Fruitier-Arnaudin I., Cohen M., Bordenave S., Sannier F., and Piot J.M. Comparative effects of angiotensin IV and two hemorphins on angiotensin-converting enzyme activity. Peptides 23 8 (2002) 1465-1470
15. Fruitier-Arnaudin I., Cohen M., Coitoux C., and Piot J.M. In vitro metabolism of LVV-hemorphin-7 by renal cytosol and purified prolyl endopeptidase. Peptides 24 (2003) 1201-1206
16. Garreau I., Cucumel K., Dagouassat N., Zhao Q., Cupo A., and Piot J.M. Hemorphin peptides are released from hemoglobin by cathepsin D. Radioimmunoassay against the C-part of V-V-hemorphin-7: an alternative assay for the cathepsin D activity. Peptides 18 2 (1997) 293-300
17. Giles A.R. Guidelines for the use of animals in biomedical research. Thromb Haemostasis 58 4 (1987) 1078-1084
18. Glamsta E.L., Marklund A., Hellman U., Wernstedt C., Terenius L., and Nyberg F. Isolation and characterization of a hemoglobin-derived opioid peptide from the human pituitary gland. Regul Pept 34 3 (1991) 169-179
19. Hayashi M.A., Murbach A.F., Ianzer D., Portaro F.C., Prezoto B.C., Fernandes B.L., et al. The C-type natriuretic peptide precursor of snake brain contains highly specific inhibitors of the angiotensin-converting enzyme. J Neurochem 85 4 (2003) 969-977
20. Hruby V.J. Designing peptide receptor agonists and antagonists. Nat Rev Drug Discov 1 (2002) 847-858
21. Ianzer D., Konno K., Marques-Porto R., Vieira Portaro F.C., Stocklin R., de Camargo A.C.M., et al. Identification of five new bradykinin potentiating peptides (BPPs) from Bothrops jararaca crude venom by using electrospray ionization tandem mass spectrometry after a two-step liquid chromatography. Peptides 25 7 (2004) 1085-1092
22. Ivanov V.T., Karelin A.A., Philippova M.M., Nazimov I.V., and Pletnev V.Z. Hemoglobin as a source of endogenous bioactive peptides: the concept of tissue-specific peptide pool. Biopolymers 43 2 (1997) 171-188
23. Jinsmaa Y., and Yoshikawa M. Release of hemorphin-5 from human hemoglobin by pancreatic elastase. Biosci Biotechnol Biochem 66 5 (2002) 1130-1132
24. Lantz I., Glamsta E.L., Talback L., and Nyberg F. Hemorphins derived from hemoglobin have an inhibitory action on angiotensin converting enzyme activity. FEBS Lett 287 1/2 (1991) 39-41
25. Lee J., Albiston L., Allen A.M., Mendelsohn F.A.G., Ping S.E., Barret G.L., et al. Effect of I.C.V. injection of AT4 receptor ligands, NLE1-angiotensin IV and LVV-hemorphin-7, on spatial learning in rats. Neuroscience 124 (2004) 341-349
26. Lew R.A., Mustafa T., Ye S., McDowall S.G., Chai S.Y., and Albiston A.L. Angiotensin AT4 ligands are potent, competitive inhibitors of insulin-regulated aminopeptidase (IRAP). J Neurochem 86 (2003) 344-350
27. Liebmann C., Schrader U., and Brantl V. Opioid receptor affinities of the blood-derived tetrapeptides hemorphin and cytochrophin. Eur J Pharmacol 166 3 (1989) 523-526
28. Moisan S., Harvey N., Beaudry G., Forzani P., Burhop K.E., Drapeau G., et al. Structural requirements and mechanism of the pressor activity of Leu-Val-Val-hemorphin-7, a fragment of hemoglobin beta-chain in rats. Peptides 19 1 (1998) 119-131
29. Moreau M.E., Garbacki N., Molinaro G., Brown N.J., Marceau F., and Adam A. The kallikrein-kinin system: current and future pharmacological targets. J Pharmacol Sci 99 1 (2005) 6-38
30. Natesh R., Schwager S.L., Sturrock E.D., and Acharya K.R. Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature 421 6922 (2003) 551-554
31. Nyberg F., Sanderson K., and Glämsta E. The hemorphins: a new class of opioid peptides derived from the blood protein hemoglobin. Biopolymers 43 (1997) 147-156
32. Oliveira M.C.F., Hirata I.Y., Chagas J.R., Boschcov P., Gomes R.A.S., Figueiredo A.F.S., et al. Intramolecularly quenched fluorogenic peptide substrates for human renin. Anal Biochem 203 (1992) 39-46
33. Pearson W.R., and Lipman D.J. Improved tools for biological sequence comparison. PNAS 85 (1988) 2444-2448
34. Pimenta D.C., Chen V.C., Chao J., Juliano M.A., and Juliano L. Alpha1-antichymotrypsin and kallistatin hydrolysis by human cathepsin D. J Protein Chem 19 5 (2000) 411-418
35. Pimenta D.C., Oliveira A., Juliano M.A., and Juliano L. Substrate specificity of human cathepsin D using internally quenched fluorescent peptides derived from reactive site loop of kallistatin. Biochim Biophys Acta 1544 1/2 (2001) 113-122
36. Piot J.M., Zhao Q., Guillochon D., Ricart G., and Thomas D. Isolation and characterization of two opioid peptides from a bovine hemoglobin peptic hydrolysate. Biochem Biophys Res Commun 189 1 (1992) 101-110
37. Rioli V., Gozzo F.C., Heimann A.S., Linardi A., Krieger J.E., Shida C.S., et al. Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme. J Biol Chem 278 10 (2003) 8547-8555
38. Sanderson K., Nyberg F., and Khalil Z. Modulation of peripheral inflammation by locally administered hemorphin-7. Inflamm Res 47 (1998) 49-55
39. Shimuta S.I., Sabia E.B., Paiva A.C.M., and Paiva T.B. Effect of stretching on the sensitivity of the guinea pig ileum to bradykinin and on its modification by bradykinin potentiating peptides. Eur J Pharmacol 70 (1981) 551-558